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Originally published In Press as doi:10.1074/jbc.M108719200 on October 11, 2001

J. Biol. Chem., Vol. 276, Issue 50, 47650-47657, December 14, 2001
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Peroxisome Proliferator-activated Receptor gamma  Ligands Inhibit Mitogenic Induction of p21Cip1 by Modulating the Protein Kinase Cdelta Pathway in Vascular Smooth Muscle Cells*

Shu WakinoDagger §, Ulrich KintscherDagger , Zhaowei LiuDagger , Sarah KimDagger , Fen YinDagger , Motoi Ohba||, Toshio Kuroki||, Axel H. Schönthal**, Willa A. HsuehDagger , and Ronald E. LawDagger Dagger Dagger

From the Dagger  Division of Endocrinology, Diabetes, and Hypertension, School of Medicine, 142-8555 UCLA, Los Angeles, California 90095, the || Institute of Molecular Oncology, Showa University, Hatanodai, Shinagawa-ku, Tokyo, Japan, and the ** Department of Molecular Microbiology and Immunology, School of Medicine, University of Southern California, Los Angeles, California 90033

The cyclin-dependent kinase inhibitor p21Cip1 is up-regulated in response to mitogenic stimulation in various cells. PPARgamma ligands troglitazone (TRO, 10 µM) and rosiglitazone (RSG, 10 µM) attenuated the induction of p21Cip1 protein by platelet-derived growth factor (PDGF) and insulin without affecting cognate mRNA levels in rat aortic smooth muscle cells (RASMC). The protein kinase Cdelta (PKCdelta ) inhibitor rottlerin also blocked the induction of p21Cip1 protein, whereas the conventional PKC isotype inhibitor Gö 6976 had no effect. Kinetic studies using the protein synthesis inhibitor cycloheximide showed that TRO, RSG, and rottlerin shortened the half-life of p21Cip1 protein. TRO, RSG, and rottlerin inhibited PDGF-induced expression of p21Cip1, but they did not affect insulin-induced expression of p21Cip1. Both ligands inhibited PKCdelta enzymatic activity in PDGF-stimulated RASMC but not in insulin-stimulated cells. Adenovirus-mediated overexpression of PKCdelta rescued the down-regulation of p21Cip1 expression both by TRO and RSG in PDGF-treated RASMC. These data suggested that the PKCdelta pathway plays a critical role in PDGF-induced expression of p21Cip1 in RASMC and may be the potential target for PPARgamma ligand effects. Src kinase-dependent tyrosine phosphorylation of PKCdelta was decreased substantially by TRO and RSG. Tyrosine phosphorylation and activation of c-Src in response to PDGF were unaffected by either PPARgamma ligand. Protein-tyrosine-phosphatase inhibitors sodium orthovanadate and dephostatin prevented PPARgamma ligand effects on PKCdelta tyrosine phosphorylation and enzymatic activity. Both inhibitors also reversed PPARgamma ligand effects on p21Cip1 expression in PDGF-treated RASMC. PPARgamma ligands enhanced protein-tyrosine-phosphatase activity in RASMC, which may be the mechanism for decreased PKCdelta tyrosine phosphorylation and activity. PPARgamma ligands regulate p21Cip1 at a post-translational level by blocking PKCdelta signaling and accelerating p21Cip1 turnover.

* This work was supported in part by National Institutes of Health Grant HL58328-03 (to W. A. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a fellowship from the Mary K. Iacocca Foundation.

Supported by a research fellowship from Gonda (Goldschmied) Diabetes Center, UCLA.

Dagger Dagger To whom correspondence should be addressed: Division of Endocrinology, Diabetes, and Hypertension, UCLA School of Medicine, Warren Hall, Second Floor, Suite 24-130, 900 Veteran Ave., Box 957073, Los Angeles, CA 90095. Tel.: 310-794-7555; Fax: 310-794-7654; E-mail: rlaw@mednet.ucla.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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